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ChemistryPhysical Chemistry

Enzyme-Encapsulated Silica Monolayers for Rapid Functionalization of a Gold Surface PREPRINT

Authors: Heather R. Luckarift; Glenn R. Johnson; Shankar Balasubramanian; Sheetal Paliwal; Aleksandr L. Simonian; AUBURN UNIV AL SAMUEL GINN COLL OF ENGINEERING
Abstract:
We report a simple and rapid method for the deposition of amorphous silica onto a gold surface. The method is based on the ability of lysozyme to mediate the formation of silica nanoparticles. A monolayer of lysozyme is deposited via non-specific binding to gold. The lysozyme then mediates the self-assembled formation of a silica monolayer. The silica formation described herein occurs on a surface plasmon resonance (SPR) gold surface and is characterized by SPR spectroscopy. The silica layer significantly increases the surface area compared to the gold substrate and is directly compatible with a detection system. The maximum surface concentration of lysozyme was found to be a monolayer of 2.6 ng/nm2 which allowed the deposition of a silica layer of a further 2 ng/mm2. For additional surface functionalization, the silica was also demonstrated to be a suitable matrix for immobilization of biomolecules. The encapsulation of organophosphate hydrolase (OPH) was demonstrated as a model system. The silica forms at ambient conditions in a reaction that allows the encapsulation of enzymes directly during silica formation. OPH was successfully encapsulated within the silica particles and a detection limit for the substrate, paraoxon, using the surface-encapsulated enzyme was found to be 20 uM.

Limitations: APPROVED FOR PUBLIC RELEASE
Description: Journal article
Pages: 9
Report Date: JUL 2006
Contract Number: F0863703C6006
Report Number: A857954
Keywords relating to this report:
*AMORPHOUS MATERIALS
*SELF ASSEMBLED MONOLAYERS
BIOMOLECULES
DEPOSITION
ENCAPSULATION
METHODOLOGY
ORGANOPHOSPHATES
REPRINTS
RESONANCE
SPECTROSCOPY
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